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Literature summary for 1.8.5.4 extracted from
- Mechanism of sulfide-quinone reductase investigated using site-directed mutagenesis and sulfur analysis (2002), Biochemistry, 41, 11552-11565.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) cells | Rhodobacter capsulatus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C127S | 1.3% activity compared to the wild type enzyme | Rhodobacter capsulatus |
| C159S | 0.5% activity compared to the wild type enzyme | Rhodobacter capsulatus |
| C353S | 0.4% activity compared to the wild type enzyme | Rhodobacter capsulatus |
| H131A | 20% activity at pH 6.5 and 27% activity at (optimum) pH 4.5 compared to the wild type enzyme | Rhodobacter capsulatus |
| H196A | 38% activity at pH 6.5 and 40% activity at (optimum) pH 6.2 compared to the wild type enzyme | Rhodobacter capsulatus |
| V300D | 11% activity compared to the wild type enzyme | Rhodobacter capsulatus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.003 | - |
decylubiquinone | mutant enzyme H196A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication | Rhodobacter capsulatus |  |
| 0.003 | - |
decylubiquinone | wild type enzyme, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication | Rhodobacter capsulatus | |
| 0.005 | - |
Sulfide | wild type enzyme, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication | Rhodobacter capsulatus | |
| 0.011 | - |
Sulfide | mutant enzyme H131A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication | Rhodobacter capsulatus | |
| 0.015 | - |
Sulfide | mutant enzyme H196A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication | Rhodobacter capsulatus | |
| 0.027 | - |
decylubiquinone | mutant enzyme H131A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication | Rhodobacter capsulatus | |
| 0.028 | - |
decylubiquinone | Km above 0.028 mM, mutant enzyme V300D, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication | Rhodobacter capsulatus | |
| 0.4 | - |
Sulfide | Km above 0.4 mM, mutant enzyme V300D, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication | Rhodobacter capsulatus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Rhodobacter capsulatus | 16020 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 48000 | - |
- |
Rhodobacter capsulatus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodobacter capsulatus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni-NTA column chromatography, gel filtration | Rhodobacter capsulatus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| sulfide + decylubiquinone | - |
Rhodobacter capsulatus | sulfur + decylubiquinol | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | - |
Rhodobacter capsulatus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SQR | - |
Rhodobacter capsulatus |
| sulfide-quinone reductase | - |
Rhodobacter capsulatus |
| sulfide:quinone oxidoreductase | - |
Rhodobacter capsulatus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.7 | - |
- |
Rhodobacter capsulatus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | the only cofactor, noncovalently bound | Rhodobacter capsulatus | |
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